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Database: UniProt
Entry: A0A166MJY8_9PEZI
LinkDB: A0A166MJY8_9PEZI
Original site: A0A166MJY8_9PEZI 
ID   A0A166MJY8_9PEZI        Unreviewed;      1061 AA.
AC   A0A166MJY8;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Nonribosomal peptide synthetase {ECO:0000313|EMBL:KZL64734.1};
GN   ORFNames=CT0861_06254 {ECO:0000313|EMBL:KZL64734.1};
OS   Colletotrichum tofieldiae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum spaethianum species complex.
OX   NCBI_TaxID=708197 {ECO:0000313|EMBL:KZL64734.1, ECO:0000313|Proteomes:UP000076552};
RN   [1] {ECO:0000313|EMBL:KZL64734.1, ECO:0000313|Proteomes:UP000076552}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=0861 {ECO:0000313|EMBL:KZL64734.1,
RC   ECO:0000313|Proteomes:UP000076552};
RA   Hacquard S., Kracher B., Hiruma K., Weinman A., Muench P., Garrido Oter R.,
RA   Ver Loren van Themaat E., Dallerey J.-F., Damm U., Henrissat B.,
RA   Lespinet O., Thon M., Kemen E., McHardy A.C., Schulze-Lefert P.,
RA   O'Connell R.J.;
RT   "Survival trade-offs in plant roots during colonization by closely related
RT   pathogenic and mutualistic fungi.";
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KZL64734.1}.
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DR   EMBL; LFIV01000257; KZL64734.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A166MJY8; -.
DR   STRING; 708197.A0A166MJY8; -.
DR   OrthoDB; 2230730at2759; -.
DR   Proteomes; UP000076552; Unassembled WGS sequence.
DR   GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR   GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR   GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR   Gene3D; 1.10.1200.10; ACP-like; 1.
DR   Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR036736; ACP-like_sf.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR   InterPro; IPR042099; ANL_N_sf.
DR   InterPro; IPR013120; Far_NAD-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR006162; Ppantetheine_attach_site.
DR   PANTHER; PTHR43439:SF2; ENZYME, PUTATIVE (JCVI)-RELATED; 1.
DR   PANTHER; PTHR43439; PHENYLACETATE-COENZYME A LIGASE; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF07993; NAD_binding_4; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR   SUPFAM; SSF47336; ACP-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
DR   PROSITE; PS50075; CARRIER; 1.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE   4: Predicted;
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076552}.
FT   DOMAIN          561..644
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
SQ   SEQUENCE   1061 AA;  118449 MW;  7A96A08F939CAD70 CRC64;
     MTTVSSPGPD FGRRLILHVI DDIAHAEPQK ECFRIPKSTE PKDGWRSISF RQYANAINTI
     AQLIVSKCGP ASSGHYPTIA YIGPNDARYV VFFAAAIKAG YKALFISPRN TNEAQMNLFD
     KTDCRAIAFP KSHESVVGPW VQANDMTTVE MMDLDTCFTD RDVTHFSYNK EFEDGEWEPL
     VVLHTSGSTG LPKPVVVRQG MLAIADGQRS LPRWHGALPW FTYLGGSLKS YFLPMPFFHA
     AALYCFIVLT IYYEVPCVFG IGERPLSSDL VVECLKYSKS TGCILPPSIL EEMSTSDQGI
     ETLGGLQLAG YGGGKLSQEA GDRLVRGGVT LANLIGATEA LPLPTYFNER RDLWQYFIFN
     TEDYGCEWRK SSDEGVYELV FVRIAKTPGL QAIFYTFPEL DEYRTSDLYK PHPGLPDHWT
     YCGRADNIIV FSNGEKLNPI TIEEVVSSHP LVKSAIVVGS QRFQPALLLE PLVHPNDSIE
     MKDLLNSIWP FVVTANKQTV GHGQINRHLI GIADRNKPFV RTDKGTKKRT ETVKLYSNEI
     ESLYMRANDM SESEMPHIDT STEDDLAQSI QTMFQVQLGI TQIGQDTDFF TAGADSLQVI
     EAVRLLRGGL RSLTSAIHTD TITTKVIYGN STPRRLARYI IRSLVSEDGY EGDTEDLNEI
     DAMKALKEKY SQGFIAAKSR RPEASEQGQT VILTGSTGTL GSYLLHQLVN SDRVKTVICL
     NRADDGGLKK QAITMTERGL STNYIDKVQF YRYDLSQPGL GLPPHVYAQL LEETDRIIHN
     AWPVNFNITV ETFEPHIRGV RNLADFAAKS KKRIAVAFVS SVSTVSGWDE TLGPVPEETI
     KDMTLPRLGY GRSKMIGSLI LEDAAKVGDF DSVIIRVSQI AGPEAAKGVW NPQEWLPSLI
     ASSLYLKALP YNLGTLNRVD WTPVETISKL ILEVTGITQS INPAELSGYF HASNPHQSTF
     EELAPVIQQY YGKDRILELV SFSEWVRRLE NTQGQGDESV DRNPGVKLLD TYRDASASNG
     TKRRPIQLDM TRTLQRSPAI REAKAVSPEL MRHWLKQWSF H
//
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